A chemical probe for lysine malonylation

Xiucong Bao; Qian Zhao; Tangpo Yang; Yi Man Eva Fung; Xiang David Li

doi:10.1002/anie.201300252

A chemical probe for lysine malonylation

Xiucong Bao, Qian Zhao, Tangpo Yang, Yi Man Eva Fung, Xiang David Li

Research output: Journal article publication › Journal article › Academic research › peer-review

62 Citations (Scopus)

Abstract

Tag! You′re it! MalAM-yne is a chemical reporter for malonylation of lysines within proteins (see scheme), a newly identified posttranslational modification. MalAM-yne is cell-permeable and metabolically incorporated into proteins in living cells. Subsequent bioorthogonal tag conjugation allows the fluorescent visualization of cellular malonylation and profiling of malonylated proteins.

Original language	English
Pages (from-to)	4883-4886
Number of pages	4
Journal	Angewandte Chemie - International Edition
Volume	52
Issue number	18
DOIs	https://doi.org/10.1002/anie.201300252
Publication status	Published - 26 Apr 2013
Externally published	Yes

Keywords

click chemistry
lysine malonylation
metabolic labeling
posttranslational modifications
protein modifications

ASJC Scopus subject areas

Catalysis
General Chemistry

More information

10.1002/anie.201300252

Cite this

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abstract = "Tag! You′re it! MalAM-yne is a chemical reporter for malonylation of lysines within proteins (see scheme), a newly identified posttranslational modification. MalAM-yne is cell-permeable and metabolically incorporated into proteins in living cells. Subsequent bioorthogonal tag conjugation allows the fluorescent visualization of cellular malonylation and profiling of malonylated proteins.",

keywords = "click chemistry, lysine malonylation, metabolic labeling, posttranslational modifications, protein modifications",

author = "Xiucong Bao and Qian Zhao and Tangpo Yang and Fung, {Yi Man Eva} and Li, {Xiang David}",

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AU - Bao, Xiucong

AU - Zhao, Qian

AU - Yang, Tangpo

AU - Fung, Yi Man Eva

AU - Li, Xiang David

PY - 2013/4/26

Y1 - 2013/4/26

N2 - Tag! You′re it! MalAM-yne is a chemical reporter for malonylation of lysines within proteins (see scheme), a newly identified posttranslational modification. MalAM-yne is cell-permeable and metabolically incorporated into proteins in living cells. Subsequent bioorthogonal tag conjugation allows the fluorescent visualization of cellular malonylation and profiling of malonylated proteins.

AB - Tag! You′re it! MalAM-yne is a chemical reporter for malonylation of lysines within proteins (see scheme), a newly identified posttranslational modification. MalAM-yne is cell-permeable and metabolically incorporated into proteins in living cells. Subsequent bioorthogonal tag conjugation allows the fluorescent visualization of cellular malonylation and profiling of malonylated proteins.

KW - click chemistry

KW - lysine malonylation

KW - metabolic labeling

KW - posttranslational modifications

KW - protein modifications

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U2 - 10.1002/anie.201300252

DO - 10.1002/anie.201300252

M3 - Journal article

C2 - 23533089

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JO - Angewandte Chemie - International Edition

JF - Angewandte Chemie - International Edition

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ER -

A chemical probe for lysine malonylation

Abstract

Keywords

ASJC Scopus subject areas

More information

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